Abstract
The TEAD transcription factors (TEAD1-4) are critical effectors of the Hippo pathway, forming active nuclear complexes with transcriptional co-activators YAP/TAZ to regulate cell growth/apoptosis pathways and control fundamental processes such as organ size. Frequent dysregulation of the Hippo pathway in cancer and the presence of druggable binding sites on TEADs make them attractive targets for development of small molecule inhibitors and degraders. Here, we identify and mechanistically characterize three unique series of bifunctional degraders that target TEAD1 via a lipid pocket and recruit different members of the Inhibitor of Apoptosis proteins (IAPs) family to effect degradation of TEAD1. We provide a detailed toolkit for structural, biophysical and cellular profiling, including the development of a cellular target engagement assay for the lipid pocket of TEAD1 and an IAP/TEAD1 ternary complex formation assay. Our study therefore provides essential resources for detailed characterization of IAP-recruiting degraders and important tools and learnings for bifunctional degraders targeted to the lipid pocket of TEADs.
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Data availability
Additional data supporting this study are available within the Supplementary Information and Supplementary Data 1–5. Coordinates and structure factors for the X-ray crystal structures have been deposited in the PDB with accession codes 9N1R (XIAP-BIR3:A171), 9N21 (XIAP-BIR3:A250) and 9N23 (cIAP1-BIR3:A273). The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD068528.
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Acknowledgements
We would like to thank Peter Ettmayer for assistance in the establishment of the joint WEHI-Boehringer Ingelheim research collaboration. We also thank Ulrich Reiser and Manfred Koegl for useful discussions. We would like to acknowledge and thank the National Drug Discovery Centre (NDDC)/WEHI Screening lab for assistance with compound dispensing, the WEHI Protein Production facility for assistance with scale-up protein production, and the staff of WEHI flow cytometry for their technical assistance and services. We would like to thank the Bio21-WEHI Crystallization Facility within the Melbourne Protein Characterization Facility, as well as the Melbourne Mass Spectrometry and Proteomics Facility, at the Bio21 Molecular Science and Biotechnology Institute, the University for Melbourne, respectively for crystallization and mass spectrometry analysis support. At the WEHI Proteomics facility, we would like to acknowledge and especially thank Sukhdeep Spall for sample processing, Vineet Vaibhav for mass spectrometry acquisitions and Laura F Dagley for her expert input and discussions. This research was undertaken in part using the MX2 beamline at the Australian Synchrotron, part of ANSTO, and made use of the Australian Cancer Research Foundation (ACRF) detector. We acknowledge use of the DepMap portal (https://depmap.org/portal). Molecular graphics and analyses were performed with UCSF ChimeraX, developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco, with support from National Institutes of Health R01-GM129325 and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases. Some figure sections were generated using Biorender.com (Fig. 1f, https://BioRender.com/kpuncmr; Fig. 5d, https://BioRender.com/bvai946 and Fig. 5e, https://BioRender.com/y5f75vs; Graphical abstract, https://BioRender.com/ojnl1ng). This research was also made possible through Victorian State Government Operational Infrastructure Support and Australian Government NHMRC IRIISS (GNT9000719) and was supported by NHMRC fellowships to John Silke (1107149, 1195038).
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J.S., D.M., I.S.L., F.M., N.E.A.C., and M.J.R. conceived the idea. M.J.R., N.E.A.C., J.S., I.S.L., F.M., H.W., and D.M. directed the project. N.T., L.D., A.T., J.B., P.G., S.K., M.J.R., and N.E.A.C. designed compounds. N.T., N.E.A.C., L.D., and M.J.R. supervised chemistry experiments. N.T., L.D., A.T., and J.B. synthesized compounds and acquired, analyzed and compiled associated analytical data. S.N. developed and performed TR-FRET assays. M.J.R. supervised biophysical experiments and developed and performed SPR assays. T.G. provided biophysical assay development and compound logistics support. S.N., M.J.R., J.S., I.S.L., and P.S. designed proteins, and S.N. and M.J.R. undertook protein crystallization experiments, interpreted, compiled and deposited structural data. G.B. contributed protein crystallography methodology. Z.J. provided computational modeling support. F.M., J.W., N.G., J.S., and M.J.R. supervised cell biology experiments. N.G., M.R., J.W., and C.B. undertook cell biology experiments. N.B. provided advice and support for cell biology screening experiments. N.G. developed and validated knockout cell lines and developed and performed degradation profiling and localization of endogenous TEAD and IAPs. J.S., M.R., M.J.R., and N.S. designed and generated cellular expression constructs. M.R., J.W., and C.B. developed HiBiT-TEAD cell lines and performed HiBiT degradation profiling. M.R. developed fluorescent cell lines and performed HiBiT degradation profiling. J.S., M.J.R., and M.R. developed and M.R. performed IAP- and TEAD-cellular target engagement and ternary complex formation assays. J.E. contributed degradation mathematical modeling support. F.M., J.W., and C.B. developed, and J.W. and C.B. performed antiproliferative, qPCR and gene reporter assays and contributed figures and text to the manuscript. For mass spectrometry proteomics run by the WEHI proteomics facility, N.G. prepared samples and undertook downstream data interpretation, and J.Y. carried out data processing and statistical analysis of raw mass spectrometry proteomics data. N.G., M.J.R., A.T., J.B., M.R., J.S., I.S.L., F.M., and N.E.A.C. co-wrote the manuscript and N.G., M.J.R., M.R., F.M., and J.Y. prepared figures, with input from all authors.
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C.B., J.W., P.G., Z.J., J.E., S.K., T.G., P.S., N.B., H.W., D.M., F.M., and N.E.A.C. are current or former employees of Boehringer Ingelheim. J.S., I.S.L., and M.J.R. have received sponsored research support from Boehringer Ingelheim.
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Gupta, N., Trainor, N., Radwan, M. et al. Expanding the toolbox to develop IAP-based degraders of TEAD transcription factors. Commun Chem (2026). https://doi.org/10.1038/s42004-025-01871-x
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DOI: https://doi.org/10.1038/s42004-025-01871-x
